Crystal structure of the tricellulin C-terminal coiled-coil domain reveals a unique mode of dimerization

被引:9
|
作者
Schuetz, Anja [1 ]
Radusheva, Veselina [1 ]
Krug, Susanne M. [2 ]
Heinemann, Udo [1 ,3 ,4 ]
机构
[1] Max Delbruck Ctr Mol Med, Helmholtz Prot Sample Prod Facil, Berlin, Germany
[2] Charite, Inst Clin Physiol, Campus Benjamin Franklin, Berlin, Germany
[3] Max Delbruck Ctr Mol Med, Macromol Struct & Interact, Robert Rossle Str 10, D-13125 Berlin, Germany
[4] Free Univ Berlin, Chem & Biochem Inst, Berlin, Germany
关键词
tight junction; tricellulin; crystal structure; CC domain; dimerization; TIGHT-JUNCTION; SECONDARY-STRUCTURE; PROTEIN; OCCLUDIN; PERMEABILITY; CONTACTS; BARRIER; IDENTIFICATION; MARVELD3; CLAUDINS;
D O I
10.1111/nyas.13408
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Tricellulin is a tight junction protein localized to tricellular contacts in many epithelial tissues, where it is required for full barrier control. Here, we present crystal structures of the tricellulin C-terminal coiled-coil domain, revealing a potential dimeric arrangement. By combining structural, biochemical, functional, and mutation analyses, we gain insight into the mode of tricellulin oligomerization and suggest a model where dimerization of its cytoplasmic C-terminus may play an auxiliary role in stabilizing homophilic and potentially also heterophilic cis-interactions within tight junctions.
引用
收藏
页码:147 / 159
页数:13
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